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SUCA_NEUCR
ID   SUCA_NEUCR              Reviewed;         333 AA.
AC   Q9P727;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Succinate--CoA ligase [ADP-forming] subunit alpha, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03222};
DE            EC=6.2.1.5 {ECO:0000255|HAMAP-Rule:MF_03222};
DE   AltName: Full=Succinyl-CoA synthetase subunit alpha {ECO:0000255|HAMAP-Rule:MF_03222};
DE            Short=SCS-alpha {ECO:0000255|HAMAP-Rule:MF_03222};
DE   Flags: Precursor;
GN   Name=tca-8 {ECO:0000303|PubMed:15522735}; ORFNames=8D4.130, NCU01227;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA   Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT   genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
RN   [3]
RP   PATHWAY.
RX   PubMed=15522735; DOI=10.1016/s0065-2660(04)52005-9;
RA   Radford A.;
RT   "Metabolic highways of Neurospora crassa revisited.";
RL   Adv. Genet. 52:165-207(2004).
CC   -!- FUNCTION: Succinyl-CoA synthetase functions in the citric acid cycle
CC       (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of ATP
CC       and thus represents the only step of substrate-level phosphorylation in
CC       the TCA. The alpha subunit of the enzyme binds the substrates coenzyme
CC       A and phosphate, while succinate binding and nucleotide specificity is
CC       provided by the beta subunit. {ECO:0000255|HAMAP-Rule:MF_03222}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + CoA + succinate = ADP + phosphate + succinyl-CoA;
CC         Xref=Rhea:RHEA:17661, ChEBI:CHEBI:30031, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292,
CC         ChEBI:CHEBI:456216; EC=6.2.1.5; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03222};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate
CC       from succinyl-CoA (ligase route): step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_03222, ECO:0000305|PubMed:15522735}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
CC       {ECO:0000255|HAMAP-Rule:MF_03222}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03222}.
CC   -!- SIMILARITY: Belongs to the succinate/malate CoA ligase alpha subunit
CC       family. {ECO:0000255|HAMAP-Rule:MF_03222}.
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DR   EMBL; AL353819; CAB88555.1; -; Genomic_DNA.
DR   EMBL; CM002240; EAA32357.1; -; Genomic_DNA.
DR   PIR; T48739; T48739.
DR   RefSeq; XP_961593.1; XM_956500.3.
DR   AlphaFoldDB; Q9P727; -.
DR   SMR; Q9P727; -.
DR   STRING; 5141.EFNCRP00000004336; -.
DR   PRIDE; Q9P727; -.
DR   EnsemblFungi; EAA32357; EAA32357; NCU01227.
DR   GeneID; 3877725; -.
DR   KEGG; ncr:NCU01227; -.
DR   VEuPathDB; FungiDB:NCU01227; -.
DR   HOGENOM; CLU_052104_1_0_1; -.
DR   InParanoid; Q9P727; -.
DR   OMA; VIICITE; -.
DR   UniPathway; UPA00223; UER00999.
DR   Proteomes; UP000001805; Chromosome 2, Linkage Group V.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0009361; C:succinate-CoA ligase complex (ADP-forming); IBA:GO_Central.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IBA:GO_Central.
DR   GO; GO:0004776; F:succinate-CoA ligase (GDP-forming) activity; IBA:GO_Central.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR   Gene3D; 3.40.50.261; -; 1.
DR   HAMAP; MF_01988; Succ_CoA_alpha; 1.
DR   InterPro; IPR017440; Cit_synth/succinyl-CoA_lig_AS.
DR   InterPro; IPR033847; Citrt_syn/SCS-alpha_CS.
DR   InterPro; IPR003781; CoA-bd.
DR   InterPro; IPR005810; CoA_lig_alpha.
DR   InterPro; IPR005811; CoA_ligase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR016102; Succinyl-CoA_synth-like.
DR   Pfam; PF02629; CoA_binding; 1.
DR   Pfam; PF00549; Ligase_CoA; 1.
DR   PIRSF; PIRSF001553; SucCS_alpha; 1.
DR   SMART; SM00881; CoA_binding; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF52210; SSF52210; 1.
DR   TIGRFAMs; TIGR01019; sucCoAalpha; 1.
DR   PROSITE; PS01216; SUCCINYL_COA_LIG_1; 1.
DR   PROSITE; PS00399; SUCCINYL_COA_LIG_2; 1.
PE   3: Inferred from homology;
KW   Ligase; Mitochondrion; Nucleotide-binding; Reference proteome;
KW   Transit peptide; Tricarboxylic acid cycle.
FT   TRANSIT         1..23
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT   CHAIN           24..333
FT                   /note="Succinate--CoA ligase [ADP-forming] subunit alpha,
FT                   mitochondrial"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT                   /id="PRO_0000260162"
FT   ACT_SITE        286
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT   BINDING         51..54
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT   BINDING         77
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT   BINDING         130..132
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT   BINDING         194
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared with subunit beta"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
SQ   SEQUENCE   333 AA;  34738 MW;  BA6FBF63AD918BDE CRC64;
     MQAIARQTRP AGKLVQQLSK RAYSSNSSPY AATINNLKIN GDTKVLFQGF TGKQGTFHAQ
     QAIEYGTNVV GGTNPKKAGQ THLDRPVFSN VSEAVKETGA TATAIFVPPP LAAAGIEEAL
     QAEIPLAVCI TEGIPQHDMV RITSMLKTQS KTRLVGPNCP GIIAPGQCKI GIMPGFIHKR
     GRIGIVSRSG TLTYEAVNQT TQAGLGQSLV VGIGGDPFSG TNFIDCLKVF LEDGDTDGII
     MIGEIGGSAE EEAADFLKEY NTKNGGKPVV SFIAGISAPP GRRMGHAGAI VAGGKGGADS
     KIKALEAAGV VVERSPASLG KALRDEFVRR DLL
 
 
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